Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility

Myosin binding protein C remained a perplexing although integral component of the sarcomeric thick filament until the discovery that genetic defects in its corresponding gene is a frequent cause of hypertrophic cardiomyopathy. Basic science investigation subsequently revealed that it is one of the m...

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Autores principales:	Amsha Ramburan, Lundi Korkie, Johanna C. Moolman-Smook
Formato:	article
Lenguaje:	EN
Publicado:	South African Heart Association 2017
Materias:	myosin binding protein c cardiac contractility Diseases of the circulatory (Cardiovascular) system RC666-701
Acceso en línea:	https://doaj.org/article/d41b372101a849ac8d99c07d15e6327d
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spelling	oai:doaj.org-article:d41b372101a849ac8d99c07d15e6327d2021-11-22T10:15:18ZCardiac myosin binding protein C, adrenergic stimulation and cardiac contractility10.24170/7-1-19661996-67412071-4602https://doaj.org/article/d41b372101a849ac8d99c07d15e6327d2017-04-01T00:00:00Zhttps://www.journals.ac.za/index.php/SAHJ/article/view/1966https://doaj.org/toc/1996-6741https://doaj.org/toc/2071-4602Myosin binding protein C remained a perplexing although integral component of the sarcomeric thick filament until the discovery that genetic defects in its corresponding gene is a frequent cause of hypertrophic cardiomyopathy. Basic science investigation subsequently revealed that it is one of the most potent regulators of cardiac contractility. Phosphorylation of its N-terminus upon adrenergic stimulation, causes increased order in myosin heads as well as increased ATPase activity, Fmax and Ca2+-sensitivity of contraction, while its dephosphorylation upon cholinergic stimulation or during low flow ischaemia leads to changes in the sarcomeric thick filament that diminish interaction between myosin heads and actin. This dynamic flux in phosphorylation upon adrenergic stimulation is not only crucial to normal cardiac function and structure, but also vital for protection against ischaemic injury. Genetically-driven deficiency or inadequacy in cMyBPC leads to severe cardiac dysfunction and structural changes, including cardiac hypertrophy and dilation, and particularly attenuates the adaptive increase in left ventricular contractility that follows on β-adrenergic stimulation or pressure overload, resulting in decreased systolic function, and reduced cardiac output.Amsha RamburanLundi KorkieJohanna C. Moolman-SmookSouth African Heart Associationarticlemyosin binding protein ccardiac contractilityDiseases of the circulatory (Cardiovascular) systemRC666-701ENSA Heart Journal, Vol 7, Iss 1, Pp 38-47 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	myosin binding protein c cardiac contractility Diseases of the circulatory (Cardiovascular) system RC666-701
spellingShingle	myosin binding protein c cardiac contractility Diseases of the circulatory (Cardiovascular) system RC666-701 Amsha Ramburan Lundi Korkie Johanna C. Moolman-Smook Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility
description	Myosin binding protein C remained a perplexing although integral component of the sarcomeric thick filament until the discovery that genetic defects in its corresponding gene is a frequent cause of hypertrophic cardiomyopathy. Basic science investigation subsequently revealed that it is one of the most potent regulators of cardiac contractility. Phosphorylation of its N-terminus upon adrenergic stimulation, causes increased order in myosin heads as well as increased ATPase activity, Fmax and Ca2+-sensitivity of contraction, while its dephosphorylation upon cholinergic stimulation or during low flow ischaemia leads to changes in the sarcomeric thick filament that diminish interaction between myosin heads and actin. This dynamic flux in phosphorylation upon adrenergic stimulation is not only crucial to normal cardiac function and structure, but also vital for protection against ischaemic injury. Genetically-driven deficiency or inadequacy in cMyBPC leads to severe cardiac dysfunction and structural changes, including cardiac hypertrophy and dilation, and particularly attenuates the adaptive increase in left ventricular contractility that follows on β-adrenergic stimulation or pressure overload, resulting in decreased systolic function, and reduced cardiac output.
format	article
author	Amsha Ramburan Lundi Korkie Johanna C. Moolman-Smook
author_facet	Amsha Ramburan Lundi Korkie Johanna C. Moolman-Smook
author_sort	Amsha Ramburan
title	Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility
title_short	Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility
title_full	Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility
title_fullStr	Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility
title_full_unstemmed	Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility
title_sort	cardiac myosin binding protein c, adrenergic stimulation and cardiac contractility
publisher	South African Heart Association
publishDate	2017
url	https://doaj.org/article/d41b372101a849ac8d99c07d15e6327d
work_keys_str_mv	AT amsharamburan cardiacmyosinbindingproteincadrenergicstimulationandcardiaccontractility AT lundikorkie cardiacmyosinbindingproteincadrenergicstimulationandcardiaccontractility AT johannacmoolmansmook cardiacmyosinbindingproteincadrenergicstimulationandcardiaccontractility
_version_	1718417763791273984

Cardiac myosin binding protein C, adrenergic stimulation and cardiac contractility

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